PT98565B - Um processo de producao de uma composicao para o tratamento da infeccao por hsv - Google Patents

Um processo de producao de uma composicao para o tratamento da infeccao por hsv Download PDF

Info

Publication number: PT98565B
Authority: PT; Portugal
Prior art keywords: hsv; polypeptide; sequences; sequence; dna
Prior art date: 1990-08-02

Application number

PT98565A

Other languages

English (en)

Portuguese (pt)

Other versions

PT98565A (pt

Inventor

Rae Lyn Burke

Rose E Sekulovich

Original Assignee

Chiron Corp

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1990-08-02

Filing date

1991-08-02

Publication date

1999-01-29

1991-08-02 Application filed by Chiron Corp filed Critical Chiron Corp

1992-06-30 Publication of PT98565A publication Critical patent/PT98565A/pt

1999-01-29 Publication of PT98565B publication Critical patent/PT98565B/pt

Links

238000000034 method Methods 0.000 title claims abstract description 65
239000000203 mixture Substances 0.000 title claims abstract description 37
238000011282 treatment Methods 0.000 title claims abstract description 23
208000009889 Herpes Simplex Diseases 0.000 title claims abstract description 16
230000008569 process Effects 0.000 title claims description 12
238000004519 manufacturing process Methods 0.000 title abstract description 8
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 120
102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 115
229920001184 polypeptide Polymers 0.000 claims abstract description 111
108010068250 Herpes Simplex Virus Protein Vmw65 Proteins 0.000 claims abstract description 109
230000002163 immunogen Effects 0.000 claims abstract description 50
108090000288 Glycoproteins Proteins 0.000 claims abstract description 44
102000003886 Glycoproteins Human genes 0.000 claims abstract description 43
241000701074 Human alphaherpesvirus 2 Species 0.000 claims description 36
239000000546 pharmaceutical excipient Substances 0.000 claims description 6
241000700584 Simplexvirus Species 0.000 abstract description 89
208000015181 infectious disease Diseases 0.000 abstract description 14
210000004027 cell Anatomy 0.000 description 63
239000013598 vector Substances 0.000 description 51
108090000623 proteins and genes Proteins 0.000 description 49
108020004414 DNA Proteins 0.000 description 38
108091033319 polynucleotide Proteins 0.000 description 33
102000040430 polynucleotide Human genes 0.000 description 33
239000002157 polynucleotide Substances 0.000 description 33
229960005486 vaccine Drugs 0.000 description 31
239000012634 fragment Substances 0.000 description 29
230000014509 gene expression Effects 0.000 description 29
240000004808 Saccharomyces cerevisiae Species 0.000 description 27
241000700605 Viruses Species 0.000 description 27
235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 26
150000001413 amino acids Chemical class 0.000 description 25
235000001014 amino acid Nutrition 0.000 description 24
235000018102 proteins Nutrition 0.000 description 23
102000004169 proteins and genes Human genes 0.000 description 23
230000003053 immunization Effects 0.000 description 19
238000002649 immunization Methods 0.000 description 19
238000009396 hybridization Methods 0.000 description 16
125000003275 alpha amino acid group Chemical group 0.000 description 15
108091026890 Coding region Proteins 0.000 description 14
241001465754 Metazoa Species 0.000 description 14
239000013604 expression vector Substances 0.000 description 14
241000700588 Human alphaherpesvirus 1 Species 0.000 description 13
ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 12
241000700618 Vaccinia virus Species 0.000 description 12
206010046865 Vaccinia virus infection Diseases 0.000 description 12
230000000295 complement effect Effects 0.000 description 12
208000007089 vaccinia Diseases 0.000 description 12
201000010099 disease Diseases 0.000 description 11
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 11
210000004962 mammalian cell Anatomy 0.000 description 11
108091003079 Bovine Serum Albumin Proteins 0.000 description 10
230000005847 immunogenicity Effects 0.000 description 10
230000003472 neutralizing effect Effects 0.000 description 10
230000010076 replication Effects 0.000 description 10
230000003612 virological effect Effects 0.000 description 10
108090000790 Enzymes Proteins 0.000 description 9
238000010276 construction Methods 0.000 description 9
230000000694 effects Effects 0.000 description 9
239000012894 fetal calf serum Substances 0.000 description 9
239000013612 plasmid Substances 0.000 description 9
239000000523 sample Substances 0.000 description 9
239000000243 solution Substances 0.000 description 9
238000012546 transfer Methods 0.000 description 9
230000009466 transformation Effects 0.000 description 9
102000004190 Enzymes Human genes 0.000 description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
-1 for example Chemical class 0.000 description 8
230000004048 modification Effects 0.000 description 8
238000012986 modification Methods 0.000 description 8
239000002773 nucleotide Substances 0.000 description 8
125000003729 nucleotide group Chemical group 0.000 description 8
239000002245 particle Substances 0.000 description 8
230000028327 secretion Effects 0.000 description 8
241000588724 Escherichia coli Species 0.000 description 7
108091028043 Nucleic acid sequence Proteins 0.000 description 7
108010076504 Protein Sorting Signals Proteins 0.000 description 7
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 7
208000027418 Wounds and injury Diseases 0.000 description 7
230000006378 damage Effects 0.000 description 7
230000001419 dependent effect Effects 0.000 description 7
230000004927 fusion Effects 0.000 description 7
208000014674 injury Diseases 0.000 description 7
238000002360 preparation method Methods 0.000 description 7
230000001681 protective effect Effects 0.000 description 7
108091008146 restriction endonucleases Proteins 0.000 description 7
238000001890 transfection Methods 0.000 description 7
241000894006 Bacteria Species 0.000 description 6
102000053602 DNA Human genes 0.000 description 6
101710182846 Polyhedrin Proteins 0.000 description 6
239000004480 active ingredient Substances 0.000 description 6
230000027455 binding Effects 0.000 description 6
238000010367 cloning Methods 0.000 description 6
238000001962 electrophoresis Methods 0.000 description 6
239000000463 material Substances 0.000 description 6
238000013518 transcription Methods 0.000 description 6
230000035897 transcription Effects 0.000 description 6
102000004594 DNA Polymerase I Human genes 0.000 description 5
108010017826 DNA Polymerase I Proteins 0.000 description 5
108700026244 Open Reading Frames Proteins 0.000 description 5
102000006601 Thymidine Kinase Human genes 0.000 description 5
108020004440 Thymidine kinase Proteins 0.000 description 5
238000010521 absorption reaction Methods 0.000 description 5
230000001154 acute effect Effects 0.000 description 5
239000002671 adjuvant Substances 0.000 description 5
230000015572 biosynthetic process Effects 0.000 description 5
238000009472 formulation Methods 0.000 description 5
108020001507 fusion proteins Proteins 0.000 description 5
102000037865 fusion proteins Human genes 0.000 description 5
239000000499 gel Substances 0.000 description 5
210000004392 genitalia Anatomy 0.000 description 5
238000003780 insertion Methods 0.000 description 5
230000037431 insertion Effects 0.000 description 5
230000006798 recombination Effects 0.000 description 5
238000005215 recombination Methods 0.000 description 5
238000012163 sequencing technique Methods 0.000 description 5
239000011780 sodium chloride Substances 0.000 description 5
208000024891 symptom Diseases 0.000 description 5
210000003501 vero cell Anatomy 0.000 description 5
241000201370 Autographa californica nucleopolyhedrovirus Species 0.000 description 4
108010078791 Carrier Proteins Proteins 0.000 description 4
241000238631 Hexapoda Species 0.000 description 4
108091034117 Oligonucleotide Proteins 0.000 description 4
HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 4
239000000427 antigen Substances 0.000 description 4
108091007433 antigens Proteins 0.000 description 4
102000036639 antigens Human genes 0.000 description 4
239000003795 chemical substances by application Substances 0.000 description 4
230000006870 function Effects 0.000 description 4
239000001963 growth medium Substances 0.000 description 4
238000011534 incubation Methods 0.000 description 4
230000000977 initiatory effect Effects 0.000 description 4
238000011081 inoculation Methods 0.000 description 4
230000003902 lesion Effects 0.000 description 4
239000002609 medium Substances 0.000 description 4
230000008961 swelling Effects 0.000 description 4
210000002845 virion Anatomy 0.000 description 4
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
WOVKYSAHUYNSMH-RRKCRQDMSA-N 5-bromodeoxyuridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(Br)=C1 WOVKYSAHUYNSMH-RRKCRQDMSA-N 0.000 description 3
229920000936 Agarose Polymers 0.000 description 3
102000007698 Alcohol dehydrogenase Human genes 0.000 description 3
108010021809 Alcohol dehydrogenase Proteins 0.000 description 3
241000700199 Cavia porcellus Species 0.000 description 3
108020004705 Codon Proteins 0.000 description 3
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
241000282412 Homo Species 0.000 description 3
102000014150 Interferons Human genes 0.000 description 3
108010050904 Interferons Proteins 0.000 description 3
101710163270 Nuclease Proteins 0.000 description 3
108091081024 Start codon Proteins 0.000 description 3
102000019197 Superoxide Dismutase Human genes 0.000 description 3
108010012715 Superoxide dismutase Proteins 0.000 description 3
208000025865 Ulcer Diseases 0.000 description 3
241000251539 Vertebrata <Metazoa> Species 0.000 description 3
108010067390 Viral Proteins Proteins 0.000 description 3
230000004913 activation Effects 0.000 description 3
125000003277 amino group Chemical group 0.000 description 3
210000004369 blood Anatomy 0.000 description 3
239000008280 blood Substances 0.000 description 3
238000004113 cell culture Methods 0.000 description 3
239000001913 cellulose Substances 0.000 description 3
229920002678 cellulose Polymers 0.000 description 3
238000010790 dilution Methods 0.000 description 3
239000012895 dilution Substances 0.000 description 3
108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 3
208000006454 hepatitis Diseases 0.000 description 3
231100000283 hepatitis Toxicity 0.000 description 3
230000001900 immune effect Effects 0.000 description 3
230000028993 immune response Effects 0.000 description 3
238000002347 injection Methods 0.000 description 3
239000007924 injection Substances 0.000 description 3
229940079322 interferon Drugs 0.000 description 3
230000001404 mediated effect Effects 0.000 description 3
239000012528 membrane Substances 0.000 description 3
108020004999 messenger RNA Proteins 0.000 description 3
244000005700 microbiome Species 0.000 description 3
238000010369 molecular cloning Methods 0.000 description 3
238000006386 neutralization reaction Methods 0.000 description 3
102000039446 nucleic acids Human genes 0.000 description 3
108020004707 nucleic acids Proteins 0.000 description 3
150000007523 nucleic acids Chemical class 0.000 description 3
230000026731 phosphorylation Effects 0.000 description 3
238000006366 phosphorylation reaction Methods 0.000 description 3
238000001742 protein purification Methods 0.000 description 3
238000003156 radioimmunoprecipitation Methods 0.000 description 3
230000009467 reduction Effects 0.000 description 3
230000001105 regulatory effect Effects 0.000 description 3
150000003839 salts Chemical class 0.000 description 3
239000011734 sodium Substances 0.000 description 3
239000000829 suppository Substances 0.000 description 3
239000000725 suspension Substances 0.000 description 3
238000013519 translation Methods 0.000 description 3
241000701447 unidentified baculovirus Species 0.000 description 3
229920001817 Agar Polymers 0.000 description 2
QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
241000701822 Bovine papillomavirus Species 0.000 description 2
102000014914 Carrier Proteins Human genes 0.000 description 2
241000700198 Cavia Species 0.000 description 2
206010057248 Cell death Diseases 0.000 description 2
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
102000004163 DNA-directed RNA polymerases Human genes 0.000 description 2
108090000626 DNA-directed RNA polymerases Proteins 0.000 description 2
241000206602 Eukaryota Species 0.000 description 2
206010048461 Genital infection Diseases 0.000 description 2
102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 2
108060003951 Immunoglobulin Proteins 0.000 description 2
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 2
241000124008 Mammalia Species 0.000 description 2
239000000020 Nitrocellulose Substances 0.000 description 2
108010038807 Oligopeptides Proteins 0.000 description 2
102000015636 Oligopeptides Human genes 0.000 description 2
101150012394 PHO5 gene Proteins 0.000 description 2
229910019142 PO4 Inorganic materials 0.000 description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 2
108020004511 Recombinant DNA Proteins 0.000 description 2
241000714474 Rous sarcoma virus Species 0.000 description 2
206010039509 Scab Diseases 0.000 description 2
108020004682 Single-Stranded DNA Proteins 0.000 description 2
229920002472 Starch Polymers 0.000 description 2
101710192321 Tegument protein VP16 Proteins 0.000 description 2
102000004142 Trypsin Human genes 0.000 description 2
108090000631 Trypsin Proteins 0.000 description 2
239000002253 acid Substances 0.000 description 2
DZBUGLKDJFMEHC-UHFFFAOYSA-N acridine Chemical compound C1=CC=CC2=CC3=CC=CC=C3N=C21 DZBUGLKDJFMEHC-UHFFFAOYSA-N 0.000 description 2
239000012190 activator Substances 0.000 description 2
239000008272 agar Substances 0.000 description 2
239000011543 agarose gel Substances 0.000 description 2
NWMHDZMRVUOQGL-CZEIJOLGSA-N almurtide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)CO[C@@H]([C@H](O)[C@H](O)CO)[C@@H](NC(C)=O)C=O NWMHDZMRVUOQGL-CZEIJOLGSA-N 0.000 description 2
229960000723 ampicillin Drugs 0.000 description 2
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
230000003321 amplification Effects 0.000 description 2
238000004458 analytical method Methods 0.000 description 2
230000000890 antigenic effect Effects 0.000 description 2
230000002238 attenuated effect Effects 0.000 description 2
238000000376 autoradiography Methods 0.000 description 2
230000001580 bacterial effect Effects 0.000 description 2
230000003115 biocidal effect Effects 0.000 description 2
239000000872 buffer Substances 0.000 description 2
239000007853 buffer solution Substances 0.000 description 2
239000001506 calcium phosphate Substances 0.000 description 2
229910000389 calcium phosphate Inorganic materials 0.000 description 2
235000011010 calcium phosphates Nutrition 0.000 description 2
210000000234 capsid Anatomy 0.000 description 2
239000002775 capsule Substances 0.000 description 2
239000000969 carrier Substances 0.000 description 2
239000013553 cell monolayer Substances 0.000 description 2
239000002299 complementary DNA Substances 0.000 description 2
238000007906 compression Methods 0.000 description 2
230000006835 compression Effects 0.000 description 2
239000013078 crystal Substances 0.000 description 2
230000009089 cytolysis Effects 0.000 description 2
238000012217 deletion Methods 0.000 description 2
230000037430 deletion Effects 0.000 description 2
229960000633 dextran sulfate Drugs 0.000 description 2
238000004520 electroporation Methods 0.000 description 2
230000008030 elimination Effects 0.000 description 2
238000003379 elimination reaction Methods 0.000 description 2
238000009585 enzyme analysis Methods 0.000 description 2
238000000605 extraction Methods 0.000 description 2
238000001502 gel electrophoresis Methods 0.000 description 2
230000002414 glycolytic effect Effects 0.000 description 2
230000036541 health Effects 0.000 description 2
238000002744 homologous recombination Methods 0.000 description 2
230000006801 homologous recombination Effects 0.000 description 2
102000018358 immunoglobulin Human genes 0.000 description 2
238000010324 immunological assay Methods 0.000 description 2
230000001976 improved effect Effects 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
238000001727 in vivo Methods 0.000 description 2
238000002955 isolation Methods 0.000 description 2
239000008101 lactose Substances 0.000 description 2
239000002502 liposome Substances 0.000 description 2
HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
239000003550 marker Substances 0.000 description 2
210000004779 membrane envelope Anatomy 0.000 description 2
229910052751 metal Inorganic materials 0.000 description 2
239000002184 metal Substances 0.000 description 2
150000002739 metals Chemical class 0.000 description 2
229930182817 methionine Natural products 0.000 description 2
230000035772 mutation Effects 0.000 description 2
229920001220 nitrocellulos Polymers 0.000 description 2
238000003199 nucleic acid amplification method Methods 0.000 description 2
230000000737 periodic effect Effects 0.000 description 2
239000010452 phosphate Substances 0.000 description 2
230000007505 plaque formation Effects 0.000 description 2
229920002401 polyacrylamide Polymers 0.000 description 2
238000001556 precipitation Methods 0.000 description 2
230000006337 proteolytic cleavage Effects 0.000 description 2
ZCCUUQDIBDJBTK-UHFFFAOYSA-N psoralen Chemical compound C1=C2OC(=O)C=CC2=CC2=C1OC=C2 ZCCUUQDIBDJBTK-UHFFFAOYSA-N 0.000 description 2
238000000746 purification Methods 0.000 description 2
230000009257 reactivity Effects 0.000 description 2
230000000306 recurrent effect Effects 0.000 description 2
238000012216 screening Methods 0.000 description 2
210000002966 serum Anatomy 0.000 description 2
239000012679 serum free medium Substances 0.000 description 2
238000001179 sorption measurement Methods 0.000 description 2
241000894007 species Species 0.000 description 2
239000008107 starch Substances 0.000 description 2
235000019698 starch Nutrition 0.000 description 2
239000000126 substance Substances 0.000 description 2
238000006467 substitution reaction Methods 0.000 description 2
238000003786 synthesis reaction Methods 0.000 description 2
238000012360 testing method Methods 0.000 description 2
238000002560 therapeutic procedure Methods 0.000 description 2
150000003568 thioethers Chemical class 0.000 description 2
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
GETQZCLCWQTVFV-UHFFFAOYSA-N trimethylamine Chemical compound CN(C)C GETQZCLCWQTVFV-UHFFFAOYSA-N 0.000 description 2
239000012588 trypsin Substances 0.000 description 2
241000701161 unidentified adenovirus Species 0.000 description 2
241001529453 unidentified herpesvirus Species 0.000 description 2
238000011144 upstream manufacturing Methods 0.000 description 2
230000029812 viral genome replication Effects 0.000 description 2
210000000605 viral structure Anatomy 0.000 description 2
238000005406 washing Methods 0.000 description 2
YYGNTYWPHWGJRM-UHFFFAOYSA-N (6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene Chemical compound CC(C)=CCCC(C)=CCCC(C)=CCCC=C(C)CCC=C(C)CCC=C(C)C YYGNTYWPHWGJRM-UHFFFAOYSA-N 0.000 description 1
108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 1
MIJDSYMOBYNHOT-UHFFFAOYSA-N 2-(ethylamino)ethanol Chemical compound CCNCCO MIJDSYMOBYNHOT-UHFFFAOYSA-N 0.000 description 1
NKDFYOWSKOHCCO-YPVLXUMRSA-N 20-hydroxyecdysone Chemical compound C1[C@@H](O)[C@@H](O)C[C@]2(C)[C@@H](CC[C@@]3([C@@H]([C@@](C)(O)[C@H](O)CCC(C)(O)C)CC[C@]33O)C)C3=CC(=O)[C@@H]21 NKDFYOWSKOHCCO-YPVLXUMRSA-N 0.000 description 1
LQILVUYCDHSGEU-UHFFFAOYSA-N 4-[(2,5-dioxopyrrol-1-yl)methyl]cyclohexane-1-carboxylic acid Chemical compound C1CC(C(=O)O)CCC1CN1C(=O)C=CC1=O LQILVUYCDHSGEU-UHFFFAOYSA-N 0.000 description 1
WOJKKJKETHYEAC-UHFFFAOYSA-N 6-Maleimidocaproic acid Chemical compound OC(=O)CCCCCN1C(=O)C=CC1=O WOJKKJKETHYEAC-UHFFFAOYSA-N 0.000 description 1
102000013563 Acid Phosphatase Human genes 0.000 description 1
108010051457 Acid Phosphatase Proteins 0.000 description 1
208000030090 Acute Disease Diseases 0.000 description 1
102000002260 Alkaline Phosphatase Human genes 0.000 description 1
108020004774 Alkaline Phosphatase Proteins 0.000 description 1
102100034044 All-trans-retinol dehydrogenase [NAD(+)] ADH1B Human genes 0.000 description 1
101710193111 All-trans-retinol dehydrogenase [NAD(+)] ADH4 Proteins 0.000 description 1
GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
101100163849 Arabidopsis thaliana ARS1 gene Proteins 0.000 description 1
208000031504 Asymptomatic Infections Diseases 0.000 description 1
241000972773 Aulopiformes Species 0.000 description 1
241000193830 Bacillus <bacterium> Species 0.000 description 1
101100178679 Caenorhabditis elegans hsp-1 gene Proteins 0.000 description 1
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
241000222122 Candida albicans Species 0.000 description 1
241000222128 Candida maltosa Species 0.000 description 1
108010039939 Cell Wall Skeleton Proteins 0.000 description 1
102100037633 Centrin-3 Human genes 0.000 description 1
241000282693 Cercopithecidae Species 0.000 description 1
241001227713 Chiron Species 0.000 description 1
KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
241000699800 Cricetinae Species 0.000 description 1
241000699802 Cricetulus griseus Species 0.000 description 1
FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
102000012410 DNA Ligases Human genes 0.000 description 1
108010061982 DNA Ligases Proteins 0.000 description 1
230000007018 DNA scission Effects 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
108090000204 Dipeptidase 1 Proteins 0.000 description 1
238000012286 ELISA Assay Methods 0.000 description 1
108010058643 Fungal Proteins Proteins 0.000 description 1
101150038242 GAL10 gene Proteins 0.000 description 1
102100024637 Galectin-10 Human genes 0.000 description 1
102100039556 Galectin-4 Human genes 0.000 description 1
108700007698 Genetic Terminator Regions Proteins 0.000 description 1
206010061978 Genital lesion Diseases 0.000 description 1
102000030595 Glucokinase Human genes 0.000 description 1
108010021582 Glucokinase Proteins 0.000 description 1
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
108010070600 Glucose-6-phosphate isomerase Proteins 0.000 description 1
102100031132 Glucose-6-phosphate isomerase Human genes 0.000 description 1
208000029433 Herpesviridae infectious disease Diseases 0.000 description 1
102000005548 Hexokinase Human genes 0.000 description 1
108700040460 Hexokinases Proteins 0.000 description 1
101000880522 Homo sapiens Centrin-3 Proteins 0.000 description 1
101000608765 Homo sapiens Galectin-4 Proteins 0.000 description 1
101001002657 Homo sapiens Interleukin-2 Proteins 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
102000000588 Interleukin-2 Human genes 0.000 description 1
108010002350 Interleukin-2 Proteins 0.000 description 1
102100024319 Intestinal-type alkaline phosphatase Human genes 0.000 description 1
101710184243 Intestinal-type alkaline phosphatase Proteins 0.000 description 1
235000014663 Kluyveromyces fragilis Nutrition 0.000 description 1
241001138401 Kluyveromyces lactis Species 0.000 description 1
241000235650 Kluyveromyces marxianus Species 0.000 description 1
241000235058 Komagataella pastoris Species 0.000 description 1
HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
229930195725 Mannitol Natural products 0.000 description 1
241000699670 Mus sp. Species 0.000 description 1
108700015872 N-acetyl-nor-muramyl-L-alanyl-D-isoglutamine Proteins 0.000 description 1
108700020354 N-acetylmuramyl-threonyl-isoglutamine Proteins 0.000 description 1
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
238000005481 NMR spectroscopy Methods 0.000 description 1
108010058846 Ovalbumin Proteins 0.000 description 1
102000004316 Oxidoreductases Human genes 0.000 description 1
108090000854 Oxidoreductases Proteins 0.000 description 1
206010033799 Paralysis Diseases 0.000 description 1
102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 1
241000235648 Pichia Species 0.000 description 1
108010020346 Polyglutamic Acid Proteins 0.000 description 1
108010039918 Polylysine Proteins 0.000 description 1
108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
241000288906 Primates Species 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
230000004570 RNA-binding Effects 0.000 description 1
208000035415 Reinfection Diseases 0.000 description 1
108091028664 Ribonucleotide Proteins 0.000 description 1
241000702670 Rotavirus Species 0.000 description 1
WINXNKPZLFISPD-UHFFFAOYSA-M Saccharin sodium Chemical compound [Na+].C1=CC=C2C(=O)[N-]S(=O)(=O)C2=C1 WINXNKPZLFISPD-UHFFFAOYSA-M 0.000 description 1
241000235070 Saccharomyces Species 0.000 description 1
235000003534 Saccharomyces carlsbergensis Nutrition 0.000 description 1
241001123227 Saccharomyces pastorianus Species 0.000 description 1
241000235347 Schizosaccharomyces pombe Species 0.000 description 1
101100097319 Schizosaccharomyces pombe (strain 972 / ATCC 24843) ala1 gene Proteins 0.000 description 1
229920002684 Sepharose Polymers 0.000 description 1
238000012300 Sequence Analysis Methods 0.000 description 1
108010071390 Serum Albumin Proteins 0.000 description 1
102000007562 Serum Albumin Human genes 0.000 description 1
238000002105 Southern blotting Methods 0.000 description 1
101000874347 Streptococcus agalactiae IgA FC receptor Proteins 0.000 description 1
UCKMPCXJQFINFW-UHFFFAOYSA-N Sulphide Chemical compound [S-2] UCKMPCXJQFINFW-UHFFFAOYSA-N 0.000 description 1
230000024932 T cell mediated immunity Effects 0.000 description 1
101710193546 Tegument protein VP16 homolog Proteins 0.000 description 1
108020005038 Terminator Codon Proteins 0.000 description 1
239000004098 Tetracycline Substances 0.000 description 1
BHEOSNUKNHRBNM-UHFFFAOYSA-N Tetramethylsqualene Natural products CC(=C)C(C)CCC(=C)C(C)CCC(C)=CCCC=C(C)CCC(C)C(=C)CCC(C)C(C)=C BHEOSNUKNHRBNM-UHFFFAOYSA-N 0.000 description 1
102000009843 Thyroglobulin Human genes 0.000 description 1
108010034949 Thyroglobulin Proteins 0.000 description 1
108700009124 Transcription Initiation Site Proteins 0.000 description 1
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
101150004685 UL48 gene Proteins 0.000 description 1
206010046555 Urinary retention Diseases 0.000 description 1
108010003533 Viral Envelope Proteins Proteins 0.000 description 1
208000036142 Viral infection Diseases 0.000 description 1
IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
241000235015 Yarrowia lipolytica Species 0.000 description 1
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
238000009825 accumulation Methods 0.000 description 1
230000021736 acetylation Effects 0.000 description 1
238000006640 acetylation reaction Methods 0.000 description 1
229960004150 aciclovir Drugs 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
230000002776 aggregation Effects 0.000 description 1
238000004220 aggregation Methods 0.000 description 1
238000013019 agitation Methods 0.000 description 1
239000002168 alkylating agent Substances 0.000 description 1
101150087698 alpha gene Proteins 0.000 description 1
WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
229910021529 ammonia Inorganic materials 0.000 description 1
210000004102 animal cell Anatomy 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
229940088710 antibiotic agent Drugs 0.000 description 1
230000005875 antibody response Effects 0.000 description 1
239000003443 antiviral agent Substances 0.000 description 1
238000013459 approach Methods 0.000 description 1
239000012298 atmosphere Substances 0.000 description 1
230000003190 augmentative effect Effects 0.000 description 1
230000010310 bacterial transformation Effects 0.000 description 1
239000011324 bead Substances 0.000 description 1
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
102000005936 beta-Galactosidase Human genes 0.000 description 1
108010005774 beta-Galactosidase Proteins 0.000 description 1
102000006635 beta-lactamase Human genes 0.000 description 1
230000001588 bifunctional effect Effects 0.000 description 1
239000011230 binding agent Substances 0.000 description 1
230000005540 biological transmission Effects 0.000 description 1
229940098773 bovine serum albumin Drugs 0.000 description 1
KDPAWGWELVVRCH-UHFFFAOYSA-N bromoacetic acid Chemical compound OC(=O)CBr KDPAWGWELVVRCH-UHFFFAOYSA-N 0.000 description 1
SNCZNSNPXMPCGN-UHFFFAOYSA-N butanediamide Chemical compound NC(=O)CCC(N)=O SNCZNSNPXMPCGN-UHFFFAOYSA-N 0.000 description 1
239000011575 calcium Substances 0.000 description 1
229910052791 calcium Inorganic materials 0.000 description 1
239000001110 calcium chloride Substances 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
244000309466 calf Species 0.000 description 1
229940095731 candida albicans Drugs 0.000 description 1
230000010261 cell growth Effects 0.000 description 1
239000013592 cell lysate Substances 0.000 description 1
210000004520 cell wall skeleton Anatomy 0.000 description 1
230000007969 cellular immunity Effects 0.000 description 1
230000008859 change Effects 0.000 description 1
239000002738 chelating agent Substances 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
230000000973 chemotherapeutic effect Effects 0.000 description 1
210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
229960005091 chloramphenicol Drugs 0.000 description 1
WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
210000000349 chromosome Anatomy 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
150000001875 compounds Chemical class 0.000 description 1
238000013270 controlled release Methods 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
229920001577 copolymer Polymers 0.000 description 1
239000007822 coupling agent Substances 0.000 description 1
230000037029 cross reaction Effects 0.000 description 1
NZNMSOFKMUBTKW-UHFFFAOYSA-N cyclohexanecarboxylic acid Chemical compound OC(=O)C1CCCCC1 NZNMSOFKMUBTKW-UHFFFAOYSA-N 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
235000018417 cysteine Nutrition 0.000 description 1
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
210000000805 cytoplasm Anatomy 0.000 description 1
230000034994 death Effects 0.000 description 1
230000022811 deglycosylation Effects 0.000 description 1
239000005547 deoxyribonucleotide Substances 0.000 description 1
125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
229960002086 dextran Drugs 0.000 description 1
239000008121 dextrose Substances 0.000 description 1
230000029087 digestion Effects 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
PRAKJMSDJKAYCZ-UHFFFAOYSA-N dodecahydrosqualene Natural products CC(C)CCCC(C)CCCC(C)CCCCC(C)CCCC(C)CCCC(C)C PRAKJMSDJKAYCZ-UHFFFAOYSA-N 0.000 description 1
229940079593 drug Drugs 0.000 description 1
239000003814 drug Substances 0.000 description 1
239000003995 emulsifying agent Substances 0.000 description 1
239000000839 emulsion Substances 0.000 description 1
238000005538 encapsulation Methods 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
239000003623 enhancer Substances 0.000 description 1
238000006911 enzymatic reaction Methods 0.000 description 1
238000001976 enzyme digestion Methods 0.000 description 1
150000002148 esters Chemical class 0.000 description 1
238000012869 ethanol precipitation Methods 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
230000008014 freezing Effects 0.000 description 1
238000007710 freezing Methods 0.000 description 1
230000002538 fungal effect Effects 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
150000004676 glycans Chemical class 0.000 description 1
102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
230000013595 glycosylation Effects 0.000 description 1
238000006206 glycosylation reaction Methods 0.000 description 1
125000001475 halogen functional group Chemical group 0.000 description 1
230000035876 healing Effects 0.000 description 1
229910001385 heavy metal Inorganic materials 0.000 description 1
108060003552 hemocyanin Proteins 0.000 description 1
230000002008 hemorrhagic effect Effects 0.000 description 1
208000002672 hepatitis B Diseases 0.000 description 1
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
102000055277 human IL2 Human genes 0.000 description 1
230000028996 humoral immune response Effects 0.000 description 1
230000004727 humoral immunity Effects 0.000 description 1
235000011167 hydrochloric acid Nutrition 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
150000004679 hydroxides Chemical class 0.000 description 1
210000001822 immobilized cell Anatomy 0.000 description 1
210000000987 immune system Anatomy 0.000 description 1
238000003018 immunoassay Methods 0.000 description 1
230000000984 immunochemical effect Effects 0.000 description 1
229940072221 immunoglobulins Drugs 0.000 description 1
230000004957 immunoregulator effect Effects 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
230000006698 induction Effects 0.000 description 1
150000007529 inorganic bases Chemical class 0.000 description 1
230000010354 integration Effects 0.000 description 1
230000003601 intercostal effect Effects 0.000 description 1
230000003834 intracellular effect Effects 0.000 description 1
238000001990 intravenous administration Methods 0.000 description 1
239000001573 invertase Substances 0.000 description 1
235000011073 invertase Nutrition 0.000 description 1
JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
JJWLVOIRVHMVIS-UHFFFAOYSA-N isopropylamine Chemical compound CC(C)N JJWLVOIRVHMVIS-UHFFFAOYSA-N 0.000 description 1
210000003292 kidney cell Anatomy 0.000 description 1
239000004816 latex Substances 0.000 description 1
229920000126 latex Polymers 0.000 description 1
150000002632 lipids Chemical class 0.000 description 1
239000007788 liquid Substances 0.000 description 1
239000006193 liquid solution Substances 0.000 description 1
239000006194 liquid suspension Substances 0.000 description 1
210000003141 lower extremity Anatomy 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
ZLNQQNXFFQJAID-UHFFFAOYSA-L magnesium carbonate Chemical compound [Mg+2].[O-]C([O-])=O ZLNQQNXFFQJAID-UHFFFAOYSA-L 0.000 description 1
239000001095 magnesium carbonate Substances 0.000 description 1
229910000021 magnesium carbonate Inorganic materials 0.000 description 1
235000019359 magnesium stearate Nutrition 0.000 description 1
238000012423 maintenance Methods 0.000 description 1
239000000594 mannitol Substances 0.000 description 1
235000010355 mannitol Nutrition 0.000 description 1
230000008774 maternal effect Effects 0.000 description 1
230000013011 mating Effects 0.000 description 1
230000008018 melting Effects 0.000 description 1
238000002844 melting Methods 0.000 description 1
MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
230000011987 methylation Effects 0.000 description 1
238000007069 methylation reaction Methods 0.000 description 1
238000000520 microinjection Methods 0.000 description 1
JMUHBNWAORSSBD-WKYWBUFDSA-N mifamurtide Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@@H](OC(=O)CCCCCCCCCCCCCCC)COP(O)(=O)OCCNC(=O)[C@H](C)NC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)OC(O)[C@@H]1NC(C)=O JMUHBNWAORSSBD-WKYWBUFDSA-N 0.000 description 1
229960005225 mifamurtide Drugs 0.000 description 1
108700007621 mifamurtide Proteins 0.000 description 1
150000007522 mineralic acids Chemical class 0.000 description 1
229940035032 monophosphoryl lipid a Drugs 0.000 description 1
238000002703 mutagenesis Methods 0.000 description 1
231100000350 mutagenesis Toxicity 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
PGSADBUBUOPOJS-UHFFFAOYSA-N neutral red Chemical compound Cl.C1=C(C)C(N)=CC2=NC3=CC(N(C)C)=CC=C3N=C21 PGSADBUBUOPOJS-UHFFFAOYSA-N 0.000 description 1
238000007899 nucleic acid hybridization Methods 0.000 description 1
210000004940 nucleus Anatomy 0.000 description 1
238000002515 oligonucleotide synthesis Methods 0.000 description 1
150000007524 organic acids Chemical class 0.000 description 1
235000005985 organic acids Nutrition 0.000 description 1
150000007530 organic bases Chemical class 0.000 description 1
229940092253 ovalbumin Drugs 0.000 description 1
210000001672 ovary Anatomy 0.000 description 1
239000006179 pH buffering agent Substances 0.000 description 1
238000004806 packaging method and process Methods 0.000 description 1
230000007030 peptide scission Effects 0.000 description 1
210000002640 perineum Anatomy 0.000 description 1
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
235000011007 phosphoric acid Nutrition 0.000 description 1
150000003016 phosphoric acids Chemical class 0.000 description 1
239000006187 pill Substances 0.000 description 1
239000013600 plasmid vector Substances 0.000 description 1
238000007747 plating Methods 0.000 description 1
229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
230000008488 polyadenylation Effects 0.000 description 1
229920001515 polyalkylene glycol Polymers 0.000 description 1
229920002643 polyglutamic acid Polymers 0.000 description 1
229920000656 polylysine Polymers 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
229920001282 polysaccharide Polymers 0.000 description 1
239000005017 polysaccharide Substances 0.000 description 1
229920000053 polysorbate 80 Polymers 0.000 description 1
230000029279 positive regulation of transcription, DNA-dependent Effects 0.000 description 1
230000004481 post-translational protein modification Effects 0.000 description 1
229910052700 potassium Inorganic materials 0.000 description 1
239000011591 potassium Substances 0.000 description 1
239000000843 powder Substances 0.000 description 1
230000002265 prevention Effects 0.000 description 1
MFDFERRIHVXMIY-UHFFFAOYSA-N procaine Chemical compound CCN(CC)CCOC(=O)C1=CC=C(N)C=C1 MFDFERRIHVXMIY-UHFFFAOYSA-N 0.000 description 1
229960004919 procaine Drugs 0.000 description 1
238000012545 processing Methods 0.000 description 1
230000020978 protein processing Effects 0.000 description 1
210000001938 protoplast Anatomy 0.000 description 1
230000002285 radioactive effect Effects 0.000 description 1
238000003127 radioimmunoassay Methods 0.000 description 1
108020003175 receptors Proteins 0.000 description 1
238000003259 recombinant expression Methods 0.000 description 1
238000011160 research Methods 0.000 description 1
230000004044 response Effects 0.000 description 1
239000002336 ribonucleotide Substances 0.000 description 1
125000002652 ribonucleotide group Chemical group 0.000 description 1
210000003705 ribosome Anatomy 0.000 description 1
229910052701 rubidium Inorganic materials 0.000 description 1
IGLNJRXAVVLDKE-UHFFFAOYSA-N rubidium atom Chemical compound [Rb] IGLNJRXAVVLDKE-UHFFFAOYSA-N 0.000 description 1
235000019515 salmon Nutrition 0.000 description 1
235000020050 sangria Nutrition 0.000 description 1
230000007017 scission Effects 0.000 description 1
238000007790 scraping Methods 0.000 description 1
238000007560 sedimentation technique Methods 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000009589 serological test Methods 0.000 description 1
238000002741 site-directed mutagenesis Methods 0.000 description 1
AWUCVROLDVIAJX-GSVOUGTGSA-N sn-glycerol 3-phosphate Chemical compound OC[C@@H](O)COP(O)(O)=O AWUCVROLDVIAJX-GSVOUGTGSA-N 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
159000000000 sodium salts Chemical class 0.000 description 1
RMLUKZWYIKEASN-UHFFFAOYSA-M sodium;2-amino-9-(2-hydroxyethoxymethyl)purin-6-olate Chemical compound [Na+].O=C1[N-]C(N)=NC2=C1N=CN2COCCO RMLUKZWYIKEASN-UHFFFAOYSA-M 0.000 description 1
239000007787 solid Substances 0.000 description 1
230000009870 specific binding Effects 0.000 description 1
229940031439 squalene Drugs 0.000 description 1
TUHBEKDERLKLEC-UHFFFAOYSA-N squalene Natural products CC(=CCCC(=CCCC(=CCCC=C(/C)CCC=C(/C)CC=C(C)C)C)C)C TUHBEKDERLKLEC-UHFFFAOYSA-N 0.000 description 1
230000004936 stimulating effect Effects 0.000 description 1
238000003756 stirring Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
229940031626 subunit vaccine Drugs 0.000 description 1
239000003826 tablet Substances 0.000 description 1
229960000814 tetanus toxoid Drugs 0.000 description 1
229960002180 tetracycline Drugs 0.000 description 1
229930101283 tetracycline Natural products 0.000 description 1
235000019364 tetracycline Nutrition 0.000 description 1
150000003522 tetracyclines Chemical class 0.000 description 1
238000010257 thawing Methods 0.000 description 1
229960002175 thyroglobulin Drugs 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
239000003104 tissue culture media Substances 0.000 description 1
238000004448 titration Methods 0.000 description 1
239000003053 toxin Substances 0.000 description 1
231100000765 toxin Toxicity 0.000 description 1
108700012359 toxins Proteins 0.000 description 1
230000002463 transducing effect Effects 0.000 description 1
238000010361 transduction Methods 0.000 description 1
230000026683 transduction Effects 0.000 description 1
238000000844 transformation Methods 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
230000010474 transient expression Effects 0.000 description 1
230000014621 translational initiation Effects 0.000 description 1
ILJSQTXMGCGYMG-UHFFFAOYSA-N triacetic acid Chemical compound CC(=O)CC(=O)CC(O)=O ILJSQTXMGCGYMG-UHFFFAOYSA-N 0.000 description 1
150000003626 triacylglycerols Chemical class 0.000 description 1
239000001226 triphosphate Substances 0.000 description 1
235000011178 triphosphate Nutrition 0.000 description 1
125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
230000036269 ulceration Effects 0.000 description 1
238000002255 vaccination Methods 0.000 description 1
210000003462 vein Anatomy 0.000 description 1
238000012795 verification Methods 0.000 description 1
229920002554 vinyl polymer Polymers 0.000 description 1
230000033041 viral attachment to host cell Effects 0.000 description 1
230000009385 viral infection Effects 0.000 description 1
238000012800 visualization Methods 0.000 description 1
238000001262 western blot Methods 0.000 description 1
239000000080 wetting agent Substances 0.000 description 1
238000002424 x-ray crystallography Methods 0.000 description 1
210000005253 yeast cell Anatomy 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/20—Antivirals for DNA viruses
- A61P31/22—Antivirals for DNA viruses for herpes viruses
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2710/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA dsDNA viruses
- C12N2710/00011—Details
- C12N2710/16011—Herpesviridae
- C12N2710/16611—Simplexvirus, e.g. human herpesvirus 1, 2
- C12N2710/16622—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Virology (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Veterinary Medicine (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Pharmacology & Pharmacy (AREA)
General Chemical & Material Sciences (AREA)
Animal Behavior & Ethology (AREA)
Chemical Kinetics & Catalysis (AREA)
Public Health (AREA)
Oncology (AREA)
Communicable Diseases (AREA)
Molecular Biology (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Genetics & Genomics (AREA)
Gastroenterology & Hepatology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Engineering & Computer Science (AREA)
Biotechnology (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Peptides Or Proteins (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)

PT98565A 1990-08-02 1991-08-02 Um processo de producao de uma composicao para o tratamento da infeccao por hsv PT98565B (pt)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US56152890A	1990-08-02	1990-08-02

Publications (2)

Publication Number	Publication Date
PT98565A PT98565A (pt)	1992-06-30
PT98565B true PT98565B (pt)	1999-01-29

Family

ID=24242345

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
PT98565A PT98565B (pt)	1990-08-02	1991-08-02	Um processo de producao de uma composicao para o tratamento da infeccao por hsv

Country Status (12)

Country	Link
US (2)	US5714152A (de)
EP (1)	EP0541692B1 (de)
JP (3)	JP3005292B2 (de)
AT (1)	ATE179614T1 (de)
CA (1)	CA2088600C (de)
DE (1)	DE69131200T2 (de)
DK (1)	DK0541692T3 (de)
ES (1)	ES2134197T3 (de)
GR (1)	GR3030834T3 (de)
IE (1)	IE912744A1 (de)
PT (1)	PT98565B (de)
WO (1)	WO1992002251A1 (de)

Families Citing this family (22)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB9105992D0 (en) *	1991-03-21	1991-05-08	Smithkline Beecham Biolog	Vaccine
GB9119940D0 (en) *	1991-09-18	1991-10-30	Hare Peter F J O	Polypeptide inhibitor of viral replication
US5965354A (en) *	1995-07-28	1999-10-12	Chiron Corporation	Herpes simplex virus diagnostics
US5980912A (en) *	1997-03-25	1999-11-09	Zonagen, Inc.	Chitosan induced immunopotentiation
CA2291010A1 (en)	1997-06-02	1998-12-10	Chiron Corporation	Herpes simplex virus vp22 vaccines and methods of use
US6087166A (en)	1997-07-03	2000-07-11	Basf Aktiengesellschaft	Transcriptional activators with graded transactivation potential
WO1999045957A2 (en) *	1998-03-09	1999-09-16	Smithkline Beecham Biologicals S.A.	Combined vaccine compositions
DK2272859T3 (en)	1998-08-07	2015-01-19	Univ Washington	Immunological herpes simplex virus antigens and methods for their use
US6860615B2 (en) *	1999-01-06	2005-03-01	Armament Systems And Procedures, Inc.	LED flashlight with integral keyring clip
US6569616B1 (en)	1999-07-29	2003-05-27	Wisconsin Alumni Research Foundation	Human cytomegalovirus glycoprotein O as a new drug target and subunit vaccine candidate
HK1044799A1 (zh)	1999-09-30	2002-11-01	University Of Washington	免疫学上重要的单纯疱疹病毒抗原
JP4519461B2 (ja)	2001-07-31	2010-08-04	ユニヴァーシティオブワシントン	免疫学的に重要な単純ヘルペスウイルス抗原およびそれを用いる方法
KR100420501B1 (ko) *	2001-09-26	2004-03-02	한국지질자원연구원	벤토나이트로부터 몬모릴로나이트 광물의 분리·회수 방법
AU2003238221A1 (en) *	2002-06-17	2003-12-31	Taro Pharmaceuticals U.S.A, Inc.	Ibuprofen suspension
JP2007505147A (ja)	2003-09-12	2007-03-08	アンティジェニクスインコーポレーテッド	単純ヘルペスウイルス感染の治療および予防用ワクチン
US8460674B2 (en)	2009-02-07	2013-06-11	University Of Washington	HSV-1 epitopes and methods for using same
WO2010115172A2 (en)	2009-04-03	2010-10-07	University Of Washington	Antigenic peptide of hsv-2 and methods for using same
EP3756684A1 (de)	2009-05-22	2020-12-30	Genocea Biosciences, Inc.	Impfstoffe gegen herpes-simplex-virus typ 2: zusammensetzungen und verfahren zur auslösung einer immunantwort
EP2643014A4 (de)	2010-11-24	2015-11-11	Genocea Biosciences Inc	Impfstoffe gegen den herpes-simplex-virus vom typ 2: zusammensetzungen und verfahren zur auslösung einer immunreaktion
EP2782597B1 (de)	2011-11-23	2022-04-13	Genocea Biosciences, Inc.	Nukleinsäureimpfstoffe gegen den herpes-simplex-virus vom typ 2: zusammensetzungen und verfahren zur auslösung einer immunreaktion
JP2019537555A (ja)	2016-09-28	2019-12-26	ジェノセアバイオサイエンシーズ，インコーポレイテッド	ヘルペスを処置するための方法および組成物
US10745931B1 (en)	2019-08-14	2020-08-18	Premises Innovations Llc	Self-rightening post system

Family Cites Families (16)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
AU1678783A (en) *	1982-07-20	1984-01-26	Molecular Genetics, Inc.	Production of herpes simplex viral proteins
US4891315A (en) *	1982-10-25	1990-01-02	American Cyanamid Company	Production of herpes simplex viral porteins
US4818694A (en) *	1982-07-20	1989-04-04	American Cyanamid Company	Production of herpes simplex viral protein
EP0133063B1 (de) *	1983-06-23	1987-01-07	Stanley Dr. Person	Immunologisch reaktive nicht-glycosilierte Aminosäureketten von Glycoprotein-B des Herpes-Virus Typ 1 und Typ 2
NZ209308A (en) *	1983-08-30	1991-08-27	Genentech Inc	Vaccine against hsv involving a truncated membrane-free derivative of a membrane-bound protein
JPS6051120A (ja) *	1983-08-31	1985-03-22	Chemo Sero Therapeut Res Inst	単純ヘルペスサブユニットワクチン
US4642333A (en) *	1983-09-16	1987-02-10	Stanley Person	Immunologically reactive non-glycosylated amino acid chains of glycoprotein B of herpes virus types 1 and 2
US4855224A (en) *	1984-03-09	1989-08-08	Genentech, Inc.	Molecularly cloned diagnostic product and method of use
US5171568A (en) *	1984-04-06	1992-12-15	Chiron Corporation	Recombinant herpes simplex gb-gd vaccine
EP0175787B1 (de) *	1984-04-06	1995-02-15	Chiron Corporation	Rekombinanter herpes simplex gb-gd impfstoff
US4618578A (en) *	1984-07-17	1986-10-21	Chiron Corporation	Expression of glycoprotein D of herpes simplex virus
FR2563434B1 (fr) *	1984-04-25	1986-07-25	Transgene Sa	Vaccin contre la rage et procede pour sa preparation
US4859587A (en) *	1984-06-04	1989-08-22	Institut Merieux	Recombinant herpes simplex viruses, vaccines and methods
JPH0668B2 (ja) *	1985-08-30	1994-01-05	財団法人化学及血清療法研究所	単純ヘルペスウイルス遺伝子が組込まれた組換えプラスミド
WO1988002634A1 (en) *	1986-10-20	1988-04-21	Chiron Corporation	Vaccine for use in the therapeutic treatment of hsv
GB8917029D0 (en) *	1989-07-25	1989-09-13	Marie Curie Memorial Foundatio	Polypeptide inhibitor of viral replication

1991
- 1991-07-30 EP EP91914945A patent/EP0541692B1/de not_active Expired - Lifetime
- 1991-07-30 JP JP3514486A patent/JP3005292B2/ja not_active Expired - Fee Related
- 1991-07-30 WO PCT/US1991/005403 patent/WO1992002251A1/en not_active Ceased
- 1991-07-30 ES ES91914945T patent/ES2134197T3/es not_active Expired - Lifetime
- 1991-07-30 AT AT91914945T patent/ATE179614T1/de not_active IP Right Cessation
- 1991-07-30 CA CA002088600A patent/CA2088600C/en not_active Expired - Fee Related
- 1991-07-30 DE DE69131200T patent/DE69131200T2/de not_active Expired - Fee Related
- 1991-07-30 DK DK91914945T patent/DK0541692T3/da active
- 1991-08-01 IE IE274491A patent/IE912744A1/en not_active Application Discontinuation
- 1991-08-02 PT PT98565A patent/PT98565B/pt not_active IP Right Cessation
1994
- 1994-10-13 US US08/322,729 patent/US5714152A/en not_active Expired - Fee Related
1995
- 1995-05-17 US US08/442,980 patent/US5795579A/en not_active Expired - Fee Related
1999
- 1999-03-23 JP JP11078661A patent/JPH11308998A/ja not_active Withdrawn
- 1999-07-21 GR GR990401924T patent/GR3030834T3/el unknown
2001
- 2001-09-10 JP JP2001274335A patent/JP2002136297A/ja not_active Withdrawn

Also Published As

Publication number	Publication date
DE69131200D1 (en)	1999-06-10
PT98565A (pt)	1992-06-30
JP3005292B2 (ja)	2000-01-31
JPH11308998A (ja)	1999-11-09
ES2134197T3 (es)	1999-10-01
JPH06502989A (ja)	1994-04-07
EP0541692A4 (en)	1993-12-08
EP0541692A1 (de)	1993-05-19
DK0541692T3 (da)	1999-11-01
EP0541692B1 (de)	1999-05-06
US5714152A (en)	1998-02-03
CA2088600C (en)	1999-11-16
US5795579A (en)	1998-08-18
WO1992002251A1 (en)	1992-02-20
GR3030834T3 (en)	1999-11-30
CA2088600A1 (en)	1992-02-03
IE912744A1 (en)	1992-02-12
ATE179614T1 (de)	1999-05-15
DE69131200T2 (de)	1999-12-09
JP2002136297A (ja)	2002-05-14

Legal Events

Date

Code

Title

Description

1992-06-30

BB1A

Laying open of patent application

Effective date: 19920218

1999-01-29

FG3A

Patent granted, date of granting

Effective date: 19981020

2004-07-30

MM3A

Annulment or lapse

Free format text: LAPSE DUE TO NON-PAYMENT OF FEES

Effective date: 20040430

Publication	Publication Date	Title
PT98565B (pt)	1999-01-29	Um processo de producao de uma composicao para o tratamento da infeccao por hsv
US5294548A (en)	1994-03-15	Recombianant Hepatitis a virus
US7045136B1 (en)	2006-05-16	Methods of immunization using recombinant poxviruses having foreign DNA expressed under the control of poxvirus regulatory sequences
JP3334876B2 (ja)	2002-10-15	組換え単純ヘルペスウイルスワクチン及び方法
JP2599350B2 (ja)	1997-04-09	膜結合性タンパク質を含有するワクチン類
Robbins et al.	1986	Pseudorabies virus gene encoding glycoprotein gIII is not essential for growth in tissue culture
US5612041A (en)	1997-03-18	Recombinant herpes simplex gD vaccine
US6207168B1 (en)	2001-03-27	Vaccine composition for herpes simplex virus and methods of using
JPH02500409A (ja)	1990-02-15	弱毒化ヘルペスウイルス、アミノ酸配列コード化外来ｄｎａ含有ヘルペスウイルス並びに同上含有ワクチン
US5824508A (en)	1998-10-20	Non-splicing variants of gp350/220
Johnson et al.	1986	Pathogenicity in mice of herpes simplex virus type 2 mutants unable to express glycoprotein C
US20130064844A1 (en)	2013-03-14	Non-splicing variants of gp350/220
US5922328A (en)	1999-07-13	Methods and compositions for treatment of HSV-2 infections and conditions
WO1990001546A1 (en)	1990-02-22	Equine herpesvirus-1 vaccine
WO1997009999A9 (en)	1997-11-06	Methods and compositions for treatment of hsv-2 infections and conditions
JP2999966B2 (ja)	2000-01-17	ＨＳＶｇＢをコードするポリヌクレオチド
WO1995029991A1 (en)	1995-11-09	A novel vzv gene, mutant vzv and immunogenic compositions
Gong	1989	Characterization of a novel EBV glycoprotein GP110 and the role of EBV glycoproteins in viral egress
JPH0544269B2 (de)	1993-07-05
MXPA01001175A (en)	2001-12-13	Attenuated equine herpesvirus